Matches in SemOpenAlex for { <https://semopenalex.org/work/W2806366302> ?p ?o ?g. }
- W2806366302 abstract "Membrane contact sites are cellular structures that mediate interorganelle exchange and communication. The two major tether proteins of the endoplasmic reticulum (ER), VAP-A and VAP-B, interact with proteins from other organelles that possess a small VAP-interacting motif, named FFAT [two phenylalanines (FF) in an acidic track (AT)]. In this study, using an unbiased proteomic approach, we identify a novel ER tether named motile sperm domain-containing protein 2 (MOSPD2). We show that MOSPD2 possesses a Major Sperm Protein (MSP) domain which binds FFAT motifs and consequently allows membrane tethering in vitro MOSPD2 is an ER-anchored protein, and it interacts with several FFAT-containing tether proteins from endosomes, mitochondria, or Golgi. Consequently, MOSPD2 and these organelle-bound proteins mediate the formation of contact sites between the ER and endosomes, mitochondria, or Golgi. Thus, we characterized here MOSPD2, a novel tethering component related to VAP proteins, bridging the ER with a variety of distinct organelles." @default.
- W2806366302 created "2018-06-13" @default.
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- W2806366302 date "2018-06-01" @default.
- W2806366302 modified "2023-10-18" @default.
- W2806366302 title "Identification of MOSPD2, a novel scaffold for endoplasmic reticulum membrane contact sites" @default.
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- W2806366302 doi "https://doi.org/10.15252/embr.201745453" @default.
- W2806366302 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6030701" @default.
- W2806366302 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/29858488" @default.
- W2806366302 hasPublicationYear "2018" @default.
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